Thioester protein crosslinks
From Proteopedia
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<StructureSection load='' size='350' side='right' caption='' scene='88/886048/Thioester1_2xi9/1'> | <StructureSection load='' size='350' side='right' caption='' scene='88/886048/Thioester1_2xi9/1'> | ||
| - | [https://en.wikipedia.org/wiki/Thioester Thioester bonds] between cysteine and glutamine sidechains can form covalent cross-links between polypeptide chains. Thioester bonds are one way that ubiquitin may be attached to proteins ([https://en.wikipedia.org/wiki/Ubiquitin ubiquitinylation]; see also [[Ubiquitin and Ubiquitination]]). Thioester bonds in [https://en.wikipedia.org/wiki/Complement_system complement proteins] C3 and C4 are involved in tagging pathogens for destruction by the immune system, via the alternate complement activation pathway. Thioester bonds occur in thioester domains (TED) of Gram-positive bacteria, where they are thought to mediate covalent adhesion of bacteria to host cells<ref name="slipknot">PMID: 30052296</ref>. Many surface proteins of Gram-positive bacteria are predicted to contain TED as well as [[isopeptide bond|isopeptide]] and ester cross-links. This family of proteins is termed <b>TIE proteins</b> for thioester, isopeptide, ester proteins<ref name="slipknot" />. | + | [https://en.wikipedia.org/wiki/Thioester Thioester bonds] between cysteine and glutamine sidechains can form covalent cross-links between polypeptide chains. |
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| + | *Thioester bonds are one way that ubiquitin may be attached to proteins ([https://en.wikipedia.org/wiki/Ubiquitin ubiquitinylation]; see also [[Ubiquitin and Ubiquitination]]). | ||
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| + | *Thioester bonds in [https://en.wikipedia.org/wiki/Complement_system complement proteins] C3 and C4 are involved in tagging pathogens for destruction by the immune system, via the alternate complement activation pathway. | ||
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| + | *Thioester bonds occur in thioester domains (TED) of Gram-positive bacteria, where they are thought to mediate covalent adhesion of bacteria to host cells<ref name="slipknot">PMID: 30052296</ref>. Many surface proteins of Gram-positive bacteria are predicted to contain TED as well as [[isopeptide bond|isopeptide]] and ester cross-links. This family of proteins is termed <b>TIE proteins</b> for thioester, isopeptide, ester proteins<ref name="slipknot" />. | ||
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</StructureSection> | </StructureSection> | ||
==References== | ==References== | ||
<references /> | <references /> | ||
Revision as of 23:52, 27 June 2021
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References
- ↑ 1.0 1.1 Miller OK, Banfield MJ, Schwarz-Linek U. A new structural class of bacterial thioester domains reveals a slipknot topology. Protein Sci. 2018 Jul 27. doi: 10.1002/pro.3478. PMID:30052296 doi:http://dx.doi.org/10.1002/pro.3478
